2018
The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments
Huehn A, Cao W, Elam WA, Liu X, De La Cruz EM, Sindelar CV. The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments. Journal Of Biological Chemistry 2018, 293: 5377-5383. PMID: 29463680, PMCID: PMC5900768, DOI: 10.1074/jbc.ac118.001843.Peer-Reviewed Original ResearchConceptsCofilin-decorated segmentsConformational changesCofilin/ADF proteinsActin-remodeling proteinsBind actin filamentsActin filament interactionsCofilin-induced changesEffects of cofilinCooperative conformational changesProtein occupancyADF proteinsCellular processesCell divisionStructure-based methodsCryo-EMActin segmentsIntracellular transportActin filamentsFilament twistCooperative bindingCofilinTwist changesActinFluorophore labelingSubunits
2016
Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits
Hocky GM, Baker JL, Bradley MJ, Sinitskiy AV, De La Cruz EM, Voth GA. Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits. The Journal Of Physical Chemistry B 2016, 120: 4558-4567. PMID: 27146246, PMCID: PMC4959277, DOI: 10.1021/acs.jpcb.6b02741.Peer-Reviewed Original ResearchConceptsActin filamentsRegulatory proteinsD-loopSite-specific mutagenesisSpecific divalent cationsFilament severingStructural bioinformaticsAdjacent subunitsAccessible conformational spaceSubunit conformationActin subunitsKey structural elementsAmino acidsLarge-scale changesConformational spaceSubunitsFilament mechanical propertiesProteinFilamentsDivalent cationsMagnesium ionsMolecular dynamics simulationsConformationSitesCofilin
2008
The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes
Cai Y, Chin HF, Lazarova D, Menon S, Fu C, Cai H, Sclafani A, Rodgers DW, De La Cruz EM, Ferro-Novick S, Reinisch KM. The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes. Cell 2008, 133: 1202-1213. PMID: 18585354, PMCID: PMC2465810, DOI: 10.1016/j.cell.2008.04.049.Peer-Reviewed Original Research